Involvement of a Glu71-Arg64 couple in the access channel for NADH in cytochrome P450nor

Fei Su; Shinya Fushinobu; Naoki Takaya; Hirofumi Shoun

doi:10.1271/bbb.68.1156

Involvement of a Glu71-Arg64 couple in the access channel for NADH in cytochrome P450nor

Fei Su, Shinya Fushinobu, Naoki Takaya, Hirofumi Shoun

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

Abstract

Putative access channel for NADH in the heme-distal pocket of cytochrome P450nor (P450nor) comprises many charged amino acid residues. Characterization of the E71A mutant protein of P450nor highlights the existence of a unique mechanism for binding NADH that depends on the salt bridge network between Glu71, Arg64 and Asp88.

Original language	English (US)
Pages (from-to)	1156-1159
Number of pages	4
Journal	Bioscience, Biotechnology and Biochemistry
Volume	68
Issue number	5
DOIs	https://doi.org/10.1271/bbb.68.1156
State	Published - May 2004
Externally published	Yes

Keywords

Cytochrome P450nor
NADH binding
Nitric oxide reductase
Salt bridge network

ASJC Scopus subject areas

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

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10.1271/bbb.68.1156

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title = "Involvement of a Glu71-Arg64 couple in the access channel for NADH in cytochrome P450nor",

abstract = "Putative access channel for NADH in the heme-distal pocket of cytochrome P450nor (P450nor) comprises many charged amino acid residues. Characterization of the E71A mutant protein of P450nor highlights the existence of a unique mechanism for binding NADH that depends on the salt bridge network between Glu71, Arg64 and Asp88.",

keywords = "Cytochrome P450nor, NADH binding, Nitric oxide reductase, Salt bridge network",

author = "Fei Su and Shinya Fushinobu and Naoki Takaya and Hirofumi Shoun",

note = "Funding Information: This study was supported by a grant-aid for scientific research from the Ministry of Education, Culture, Sports, Science and Technology of Japan (to HS, no. 14104005) and by the national project on protein structural and functional analysis.",

year = "2004",

month = may,

doi = "10.1271/bbb.68.1156",

language = "English (US)",

volume = "68",

pages = "1156--1159",

journal = "Bioscience, Biotechnology and Biochemistry",

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T1 - Involvement of a Glu71-Arg64 couple in the access channel for NADH in cytochrome P450nor

AU - Su, Fei

AU - Fushinobu, Shinya

AU - Takaya, Naoki

AU - Shoun, Hirofumi

N1 - Funding Information: This study was supported by a grant-aid for scientific research from the Ministry of Education, Culture, Sports, Science and Technology of Japan (to HS, no. 14104005) and by the national project on protein structural and functional analysis.

PY - 2004/5

Y1 - 2004/5

N2 - Putative access channel for NADH in the heme-distal pocket of cytochrome P450nor (P450nor) comprises many charged amino acid residues. Characterization of the E71A mutant protein of P450nor highlights the existence of a unique mechanism for binding NADH that depends on the salt bridge network between Glu71, Arg64 and Asp88.

AB - Putative access channel for NADH in the heme-distal pocket of cytochrome P450nor (P450nor) comprises many charged amino acid residues. Characterization of the E71A mutant protein of P450nor highlights the existence of a unique mechanism for binding NADH that depends on the salt bridge network between Glu71, Arg64 and Asp88.

KW - Cytochrome P450nor

KW - NADH binding

KW - Nitric oxide reductase

KW - Salt bridge network

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SN - 0916-8451

VL - 68

SP - 1156

EP - 1159

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

IS - 5

ER -

Involvement of a Glu71-Arg64 couple in the access channel for NADH in cytochrome P450nor

Abstract

Keywords

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